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Isolation and characterization of dipeptidyl peptidase IV from human meconium
Author(s) -
Caporale Carlo,
Fontanella Angiola,
Petrilli Pasquale,
Pucci Piero,
Molinaro Maria Francesca,
Picone Delia,
Auricchio Salvatore
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80621-9
Subject(s) - dipeptidyl peptidase , meconium , aminopeptidase , isolation (microbiology) , chemistry , dipeptidyl peptidase 4 , biochemistry , enzyme , biology , endocrinology , bioinformatics , amino acid , leucine , fetus , pregnancy , diabetes mellitus , type 2 diabetes , genetics
Dipeptidyl aminopeptidase IV (DAP‐IV) (EC 3.4.14.1) was purified from meconium particles sedimenting at 105000 × g . Its molecular properties and activity on synthetic and natural substrates (casomorphin and procasomorphin) were investigated.